Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli.

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Abstract
A soluble enzyme activity which catalyzes the synthesis of acyl-acyl carrier protein from acyl carrier proteins, a long chain fatty acid and ATP was demonstrated in E. coli. The reaction requires high concentrations of Ca2+ and Mg2+ for activity, and cleaves ATP and AMP and PPi. The fatty acyl product was identified as acyl-acyl carrier protein by its solubility, thioester linkage, molecular weight charge and biological activity. Several criteria indicate the enzyme is distinct from acyl-CoA synthetase. The fatty acid specificity of the enzyme suggests a role of acyl-acyl carrier protein synthetase in the incorporation of fatty acids into phospholipid.